Research workbench
AlphaFold monomer V2.0 prediction for vacuolar membrane protease (A7F4S1)
Analyse AlphaFold monomer V2.0 prediction for vacuolar membrane protease (A7F4S1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7F4S1
- Type
- protein
- Length
- 1,076 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Vacuolar membrane protease
- UniProt
- A7F4S1
- Pockets
- 13 · best druggability 0.82
Structure
1 distinct chain · 36% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protease | protein | 1076 | 36% helix, 16% strand | A7F4S1 |
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 823 | 0.82 | 0.85 | 75 | empty |
| 2 | 305 | 0.65 | 0.80 | 26 | empty |
| 3 | 56 | 0.63 | 0.93 | 18 | empty |
| 4 | 253 | 0.61 | 0.80 | 30 | empty |
| 5 | 193 | 0.59 | 0.81 | 30 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A7F4S1
- Elsewhere: UniProt A7F4S1 · AlphaFold DB A7F4S1
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